Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes.

Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Research Abstract Details 

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Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Abstract Text:

N Harada,T Omura,

1. The subcellular distribution of nitrobenzene reduction activity in rat liver cells indicated the existence of two different enzyme systems, one localized in microsomes and the other localized in cytosol. The activity in the cytosol was mainly attributable to xanthine oxidase, judging from its substrate specificity and the inhibition by allopurinol. 2. The participation of the microsomal electron transport system in nitrobenzene reduction was examined by using antibodies against four components of the system, NADPH-cytochrome c reductase (fpT), NADH-cytochrome b5 reductase (fpD), cytochrome b5, and cytochrome P-450. Both NADH- and NADPH-dependent nitrobenzene reduction activities were strongly inhibited by anti-fpT IG and also by anti-P450 IG, but not inhibited by anti-fpD IG or anti-b5 IG. The reduction of nitrosobenzene and phenylhydroxylamine, which are supposed to be the intermediates of nitrobenzene reduction, was also examined, and it was found that NADH- and NADPH-dependent reduction of both compounds were strongly inhibited by anti-fpT IG and anti-P450 IG, but not by anti-fpD IG or anti-b5 IG. 3. Reconstruction experiments using purified NADPH-cytochrome P-450 reductase and cytochrome P-450 were also carried out and it was confirmed that the reduction of nitrobenzene, nitrosobenzene, and phenylhydroxylamine to aniline could be effected by these two components. 4. Nitrobenzene reduction by microsomes exhibited a short initial time lag and was activated by the addition of purified NADPH-cytochrome c reductase, whereas nitrosobenzene and phenylhydroxylamine reductions did not show any initial time lag and were not activated by the reductase. These observations suggest that the reduction of nitrobenzene to an intermediate, possibly nitrosobenzene or phenylhydroxylamine, limits the rate of aniline formation, and such an initial step of nitrobenzene reduction can be catalyzed by NADPH-cytochrome c reductase alone. Cytochrome P-450 is essential at least in the final step of nitrobenzene reduction to aniline. This conclusion was further confirmed by determination of these intermediates in nitrobenzene reduction.

Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Publishing Authors By Initials

N Harada,T Omura,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: substrate specificity research

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Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 87

Page Numbers: 1539-54

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 1980

Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Keywords Mesh Terms:

KEYWORDS: Substrate Specificity

MESH TERMS: metabolism

Chemical & Substance for Abstract: Participation of cytochrome P-450 in the reduction of nitro compounds by rat liver microsomes. Information

Substance Name: Cytochrome Reductases

Registry Number: EC 1.6.2.-

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Country: JAPAN

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MEDLINETA: J Biochem

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